Dimethylamine dehydrogenase
From Wikipedia, the free encyclopedia
In enzymology, a dimethylamine dehydrogenase (EC 1.5.8.1) is an enzyme that catalyzes the chemical reaction
- dimethylamine + H2O + electron-transferring flavoprotein methylamine + formaldehyde + reduced electron-transferring flavoprotein
The 3 substrates of this enzyme are dimethylamine, H2O, and electron-transferring flavoprotein, whereas its 3 products are methylamine, formaldehyde, and reduced electron-transferring flavoprotein.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with a flavin as acceptor. The systematic name of this enzyme class is dimethylamine:electron-transferring flavoprotein oxidoreductase. This enzyme participates in methane metabolism. It employs one cofactor, FMN.
[edit] References
- IUBMB entry for 1.5.8.1
- BRENDA references for 1.5.8.1 (Recommended.)
- PubMed references for 1.5.8.1
- PubMed Central references for 1.5.8.1
- Google Scholar references for 1.5.8.1
- Yang CC, Packman LC, Scrutton NS (1995). "The primary structure of Hyphomicrobium X dimethylamine dehydrogenase. Relationship to trimethylamine dehydrogenase and implications for substrate recognition". Eur. J. Biochem. 232: 264–71. PMID 7556160.